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Information on EC 3.5.4.3 - guanine deaminase and Organism(s) Bacillus subtilis and UniProt Accession O34598

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.3 guanine deaminase
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This record set is specific for:
Bacillus subtilis
UNIPROT: O34598 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
guanase, guanine deaminase, cypin, agdap, guanine aminohydrolase, ne0047, cytosolic psd-95 interactor, gdease, human guanine deaminase, e. coli guanine deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDEase
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guanase
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guanine aminase
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Guanine aminohydrolase
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p51-nedasin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
guanine + H2O = xanthine + NH3
show the reaction diagram
mechanism
guanine + H2O = xanthine + NH3
show the reaction diagram
catalytic mechanism, quantum mechanical calculations using multilayered ONIOM and molecular dynamics study, the active-site residues of the enzyme do not affect the tautomeric state of guanine, Glu55 and Asp114 play important roles in proton shuttling in the reaction, proton transfer from a Zn-bound water to protonate Asp114, which can then transfer its proton to the N3 of the bound guanine, facilitating the nucleophilic attack on C2 of the guanine by the Zn-bound hydroxide to form a tetrahedral intermediate. Glu55 then transfers a proton from the Zn-hydroxide to the amino group of the reaction intermediate, ammonia leaves the active site, and xanthine is freed by the cleavage of the Zn-O2 bond
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
guanine aminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9033-16-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
guanine + H2O
xanthine + NH3
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guanine + H2O
xanthine + NH3
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
essential, surrounding ligands are H53, C83, C86
Zn2+
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a zinc metalloenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hypoxanthine
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
intertwined dimer, crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in absence and presence of inhibitor hypoxanthine, growth of crystals in 30% polyethylene glycol
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liaw, S.H.; Chang, Y.J.; Lai, C.T.; Chang, H.C.; Chang, G.G.
Crystal structure of Bacillus subtilis guanine deaminase: the first domain-swapped structure in the cytidine deaminase superfamily
J. Biol. Chem.
279
35479-35485
2004
Bacillus subtilis (O34598), Bacillus subtilis
Manually annotated by BRENDA team
Chang Yu Ju, C.Y.; Huang Chun Hsian, H.C.; Hu Chih Yun, H.C.; Liaw Shwu Hue, L.S.
Crystallization and preliminary crystallographic analysis of Bacillus subtilis guanine deaminase
Acta Crystallogr. Sect. D
60
1152-1154
2004
Bacillus subtilis
Manually annotated by BRENDA team
Yao, L.; Cukier, R.I.; Yan, H.
Catalytic mechanism of guanine deaminase: an ONIOM and molecular dynamics study
J. Phys. Chem. B
111
4200-4210
2007
Bacillus subtilis
Manually annotated by BRENDA team